메뉴 건너뛰기




Volumn 93, Issue 4, 2005, Pages 875-882

Elevation of the Hsp70 chaperone does not effect toxicity in mouse models of familial amyotrophic lateral sclerosis

Author keywords

Heat shock protein 70; Motor neuron death; Neurodegenerative disease; Protein aggregates; Stress response

Indexed keywords

CHAPERONE; COPPER ZINC SUPEROXIDE DISMUTASE; GENE PRODUCT; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90;

EID: 18844444198     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2005.03054.x     Document Type: Article
Times cited : (84)

References (37)
  • 1
    • 0037444446 scopus 로고    scopus 로고
    • Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein
    • Adachi H., Katsuno M., Minamiyama M. et al. (2003) Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein. J. Neurosci. 23, 2203-2211.
    • (2003) J. Neurosci. , vol.23 , pp. 2203-2211
    • Adachi, H.1    Katsuno, M.2    Minamiyama, M.3
  • 2
    • 0038446777 scopus 로고    scopus 로고
    • Sixteen novel mutations in the Cu/Zn superoxide dismutase gene in amyotrophic lateral sclerosis: A decade of discoveries, defects and disputes
    • Andersen P. M., Sims K. B., Xin W. W. et al. (2003) Sixteen novel mutations in the Cu/Zn superoxide dismutase gene in amyotrophic lateral sclerosis: a decade of discoveries, defects and disputes. Amyotroph. Lateral Scler. Other Motor Neuron Disord. 4, 62-73.
    • (2003) Amyotroph. Lateral Scler. Other Motor Neuron Disord. , vol.4 , pp. 62-73
    • Andersen, P.M.1    Sims, K.B.2    Xin, W.W.3
  • 3
    • 0027359404 scopus 로고
    • Isolation of Hsp90 mutants by screening for decreased steroid receptor function
    • Bohen S. P. and Yamamoto K. R. (1993) Isolation of Hsp90 mutants by screening for decreased steroid receptor function. Proc. Natl Acad. Sci. USA 90, 1I 424-1I 428.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90
    • Bohen, S.P.1    Yamamoto, K.R.2
  • 4
    • 0027965073 scopus 로고
    • Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity
    • Borchelt D. R., Lee M. K., Slunt H. S. et al. (1994) Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity. Proc. Natl Acad. Sci. USA 91, 8292-8296.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8292-8296
    • Borchelt, D.R.1    Lee, M.K.2    Slunt, H.S.3
  • 5
    • 0344507132 scopus 로고    scopus 로고
    • Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis
    • Bruening W., Roy J., Giasson B., Figlewicz D. A., Mushynski W. E. and Durham H. D. (1999) Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis. J. Neurochem. 72, 693-699.
    • (1999) J. Neurochem. , vol.72 , pp. 693-699
    • Bruening, W.1    Roy, J.2    Giasson, B.3    Figlewicz, D.A.4    Mushynski, W.E.5    Durham, H.D.6
  • 6
    • 0031051485 scopus 로고    scopus 로고
    • ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions
    • Bruijn L. I., Becher M. W., Lee M. K. et al. (1997) ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Neuron 18, 327-338.
    • (1997) Neuron , vol.18 , pp. 327-338
    • Bruijn, L.I.1    Becher, M.W.2    Lee, M.K.3
  • 8
    • 0141642203 scopus 로고    scopus 로고
    • Wild-type nonneuronal cells extend survival of SOD1 mutant motor neurons in ALS mice
    • Clement A. M., Nguyen M. D., Roberts E. A. et al. (2003) Wild-type nonneuronal cells extend survival of SOD1 mutant motor neurons in ALS mice. Science 302, 113-117.
    • (2003) Science , vol.302 , pp. 113-117
    • Clement, A.M.1    Nguyen, M.D.2    Roberts, E.A.3
  • 9
    • 0035516124 scopus 로고    scopus 로고
    • From Charcot to Lou Gehrig: Deciphering selective motor neuron death in ALS
    • Cleveland D. W. and Rothstein J. D. (2001) From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS. Nat. Rev. Neurosci. 2, 806-819.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 806-819
    • Cleveland, D.W.1    Rothstein, J.D.2
  • 10
    • 0035394668 scopus 로고    scopus 로고
    • Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice
    • Cummings C. J., Sun Y., Opal P., Antalffy B., Mestril R., Orr H. T., Dillmann W. H. and Zoghbi H. Y. (2001) Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice. Hum. Mol. Genet. 10, 1511-1518.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1511-1518
    • Cummings, C.J.1    Sun, Y.2    Opal, P.3    Antalffy, B.4    Mestril, R.5    Orr, H.T.6    Dillmann, W.H.7    Zoghbi, H.Y.8
  • 11
    • 0030777650 scopus 로고    scopus 로고
    • Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS
    • Durham H. D., Roy J., Dong L. and Figlewicz D. A. (1997) Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS. J. Neuropathol. Exp. Neurol. 56, 523-530.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 523-530
    • Durham, H.D.1    Roy, J.2    Dong, L.3    Figlewicz, D.A.4
  • 12
    • 0028284779 scopus 로고
    • Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation
    • Gumey M. E., Pu H., Chiu A. Y. et al. (1994) Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation. Science 264, 1772-1775.
    • (1994) Science , vol.264 , pp. 1772-1775
    • Gumey, M.E.1    Pu, H.2    Chiu, A.Y.3
  • 13
    • 0347928859 scopus 로고    scopus 로고
    • Overexpression of heat shock protein 70 in R6/2 Huntington's disease mice has only modest effects on disease progression
    • Hansson O., Nylandsted J., Castilho R. F., Leist M., Jaattela M. and Brundin P. (2003) Overexpression of heat shock protein 70 in R6/2 Huntington's disease mice has only modest effects on disease progression. Brain Res. 970, 47-57.
    • (2003) Brain Res. , vol.970 , pp. 47-57
    • Hansson, O.1    Nylandsted, J.2    Castilho, R.F.3    Leist, M.4    Jaattela, M.5    Brundin, P.6
  • 14
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • Hendrick J. P. and Hartl F. U. (1993) Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem. 62, 349-384.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.U.2
  • 15
    • 0037022339 scopus 로고    scopus 로고
    • Focal loss of the glutamate transporter EAAT2 in a transgenic rat model of SOD1 mutant-mediated amyotrophic lateral sclerosis (ALS)
    • Howland D. S., Liu J., She Y. et al. (2002) Focal loss of the glutamate transporter EAAT2 in a transgenic rat model of SOD1 mutant-mediated amyotrophic lateral sclerosis (ALS). Proc. Natl Acad. Sci. USA 99, 1604-1609.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1604-1609
    • Howland, D.S.1    Liu, J.2    She, Y.3
  • 16
    • 0034629073 scopus 로고    scopus 로고
    • Genetic suppression of polyglutamine toxicity in Drosophila
    • Kazemi-Esfarjani P. and Benzer S. (2000) Genetic suppression of polyglutamine toxicity in Drosophila. Science 287, 1837-1840.
    • (2000) Science , vol.287 , pp. 1837-1840
    • Kazemi-Esfarjani, P.1    Benzer, S.2
  • 17
    • 1942486792 scopus 로고    scopus 로고
    • Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice
    • Kieran D., Kalmar B., Dick J. R., Riddoch-Contreras J., Burnstock G. and Greensmith L. (2004) Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice. Nat. Med. 10, 402-405.
    • (2004) Nat. Med. , vol.10 , pp. 402-405
    • Kieran, D.1    Kalmar, B.2    Dick, J.R.3    Riddoch-Contreras, J.4    Burnstock, G.5    Greensmith, L.6
  • 18
    • 3242701496 scopus 로고    scopus 로고
    • Toxicity of familial ALS-linked SOD1 mutants from selective recruitment to spinal mitochondria
    • Liu J., Lillo C., Jonsson P. A. et al. (2004) Toxicity of familial ALS-linked SOD1 mutants from selective recruitment to spinal mitochondria. Neuron 43, 5-17.
    • (2004) Neuron , vol.43 , pp. 5-17
    • Liu, J.1    Lillo, C.2    Jonsson, P.A.3
  • 19
    • 0028932259 scopus 로고
    • Overexpression of the rat inducible 70-kD heat stress protein in a transgenic mouse increases the resistance of the heart to ischemic injury
    • Marber M. S., Mestril R., Chi S. H., Sayen M. R., Yellon D. M. and Dillmann W. H. (1995) Overexpression of the rat inducible 70-kD heat stress protein in a transgenic mouse increases the resistance of the heart to ischemic injury. J. Clin. Invest. 95, 1446-1456.
    • (1995) J. Clin. Invest. , vol.95 , pp. 1446-1456
    • Marber, M.S.1    Mestril, R.2    Chi, S.H.3    Sayen, M.R.4    Yellon, D.M.5    Dillmann, W.H.6
  • 21
    • 0035575761 scopus 로고    scopus 로고
    • Rats expressing human cytosolic copper-zinc superoxide dismutase transgenes with amyotrophic lateral sclerosis: Associated mutations develop motor neuron disease
    • Nagai M., Aoki M., Miyoshi I., Kato M., Pasinelli P., Kasai N., Brown R. H. Jr and Itoyama Y. (2001) Rats expressing human cytosolic copper-zinc superoxide dismutase transgenes with amyotrophic lateral sclerosis: associated mutations develop motor neuron disease. J. Neurosci. 21, 9246-9254.
    • (2001) J. Neurosci. , vol.21 , pp. 9246-9254
    • Nagai, M.1    Aoki, M.2    Miyoshi, I.3    Kato, M.4    Pasinelli, P.5    Kasai, N.6    Brown Jr., R.H.7    Itoyama, Y.8
  • 22
    • 0028815433 scopus 로고
    • Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons
    • Pardo C. A., Xu Z., Borchelt D. R., Price D. L., Sisodia S. S. and Cleveland D. W. (1995) Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons. Proc. Natl Acad. Sci. USA 92, 954-958.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 954-958
    • Pardo, C.A.1    Xu, Z.2    Borchelt, D.R.3    Price, D.L.4    Sisodia, S.S.5    Cleveland, D.W.6
  • 23
    • 3242703300 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria
    • Pasinelli P., Belford M. E., Lennon N., Bacskai B. J., Hyman B. T., Trotti D. and Brown R. H. Jr (2004) Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria. Neuron 43, 19-30.
    • (2004) Neuron , vol.43 , pp. 19-30
    • Pasinelli, P.1    Belford, M.E.2    Lennon, N.3    Bacskai, B.J.4    Hyman, B.T.5    Trotti, D.6    Brown Jr., R.H.7
  • 24
    • 17744372861 scopus 로고    scopus 로고
    • Roles of the heat shock transcription factors in regulation of the heat shock response and beyond
    • Pirkkala L., Nykanen P. and Sistonen L. (2001) Roles of the heat shock transcription factors in regulation of the heat shock response and beyond. FASEB J. 15, 1118-1131.
    • (2001) FASEB J. , vol.15 , pp. 1118-1131
    • Pirkkala, L.1    Nykanen, P.2    Sistonen, L.3
  • 26
    • 0028046847 scopus 로고
    • Mitochondrial protein import: Biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44
    • Rassow J., Maarse A. C., Krainer E., Kubrich M., Muller H., Meijer M., Craig E. A. and Pfanner N. (1994) Mitochondrial protein import: biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44. J. Cell Biol. 127, 1547-1556.
    • (1994) J. Cell Biol. , vol.127 , pp. 1547-1556
    • Rassow, J.1    Maarse, A.C.2    Krainer, E.3    Kubrich, M.4    Muller, H.5    Meijer, M.6    Craig, E.A.7    Pfanner, N.8
  • 27
    • 15844393658 scopus 로고    scopus 로고
    • Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury
    • Reaume A. G., Elliott J. L., Huffman E. K. et al. (1996) Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nat. Genet. 13, 43-47.
    • (1996) Nat. Genet. , vol.13 , pp. 43-47
    • Reaume, A.G.1    Elliott, J.L.2    Huffman, E.K.3
  • 28
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen D. R., Siddique T., Patterson D. et al. (1993) Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362, 59-62.
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1    Siddique, T.2    Patterson, D.3
  • 29
    • 0032402093 scopus 로고    scopus 로고
    • Glutamate potentiates the toxicity of mutant Cu/Zn-superoxide dismutase in motor neurons by postsynaptic calcium-dependent mechanisms
    • Roy J., Minotti S., Dong L., Figlewicz D. A. and Durham H. D. (1998) Glutamate potentiates the toxicity of mutant Cu/Zn-superoxide dismutase in motor neurons by postsynaptic calcium-dependent mechanisms. J. Neurosci. 18, 9673-9684.
    • (1998) J. Neurosci. , vol.18 , pp. 9673-9684
    • Roy, J.1    Minotti, S.2    Dong, L.3    Figlewicz, D.A.4    Durham, H.D.5
  • 30
    • 0028618296 scopus 로고
    • Protein folding and the regulation of signaling pathways
    • Rutherford S. L. and Zuker C. S. (1994) Protein folding and the regulation of signaling pathways. Cell 79, 1129-1132.
    • (1994) Cell , vol.79 , pp. 1129-1132
    • Rutherford, S.L.1    Zuker, C.S.2
  • 31
    • 0035918258 scopus 로고    scopus 로고
    • Mutant Cu/Zn-superoxide dismutase proteins have altered solubility and interact with heat shock/stress proteins in models of amyotrophic lateral sclerosis
    • Shinder G. A., Lacourse M. C., Minotti S. and Durham H. D. (2001) Mutant Cu/Zn-superoxide dismutase proteins have altered solubility and interact with heat shock/stress proteins in models of amyotrophic lateral sclerosis. J. Biol. Chem. 276, 12 791-12 796.
    • (2001) J. Biol. Chem. , vol.276
    • Shinder, G.A.1    Lacourse, M.C.2    Minotti, S.3    Durham, H.D.4
  • 33
    • 0036076642 scopus 로고    scopus 로고
    • Fibrillar inclusions and motor neuron degeneration in transgenic mice expressing superoxide dismutase 1 with a disrupted copper-binding site
    • Wang J., Xu G., Gonzales V., Coonfield M., Fromholt D., Copeland N. G., Jenkins N. A. and Borchelt D. R. (2002) Fibrillar inclusions and motor neuron degeneration in transgenic mice expressing superoxide dismutase 1 with a disrupted copper-binding site. Neurobiol. Dis. 10, 128-138.
    • (2002) Neurobiol. Dis. , vol.10 , pp. 128-138
    • Wang, J.1    Xu, G.2    Gonzales, V.3    Coonfield, M.4    Fromholt, D.5    Copeland, N.G.6    Jenkins, N.A.7    Borchelt, D.R.8
  • 34
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP 70
    • Warrick J. M., Chan H. Y., Gray-Board G. L., Chai Y., Paulson H. L. and Bonini N. M. (1999) Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP 70. Nat. Genet. 23, 425-428.
    • (1999) Nat. Genet. , vol.23 , pp. 425-428
    • Warrick, J.M.1    Chan, H.Y.2    Gray-Board, G.L.3    Chai, Y.4    Paulson, H.L.5    Bonini, N.M.6
  • 35
    • 0035664213 scopus 로고    scopus 로고
    • Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues
    • Watanabe M., Dykes-Hoberg M., Culotta V. C., Price D. L., Wong P. C. and Rothstein J. D. (2001) Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues. Neurobiol. Dis 8, 933-941.
    • (2001) Neurobiol. Dis , vol.8 , pp. 933-941
    • Watanabe, M.1    Dykes-Hoberg, M.2    Culotta, V.C.3    Price, D.L.4    Wong, P.C.5    Rothstein, J.D.6
  • 36
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • Wong P. C., Pardo C. A., Borchelt D. R., Lee M. K., Copeland N. G., Jenkins N. A., Sisodia S. S., Cleveland D. W. and Price D. L. (1995) An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 14, 1105-1116.
    • (1995) Neuron , vol.14 , pp. 1105-1116
    • Wong, P.C.1    Pardo, C.A.2    Borchelt, D.R.3    Lee, M.K.4    Copeland, N.G.5    Jenkins, N.A.6    Sisodia, S.S.7    Cleveland, D.W.8    Price, D.L.9
  • 37
    • 0037428164 scopus 로고    scopus 로고
    • Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
    • Young J. C., Hoogenraad N. J. and Hartl F. U. (2003) Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 112, 41-50.
    • (2003) Cell , vol.112 , pp. 41-50
    • Young, J.C.1    Hoogenraad, N.J.2    Hartl, F.U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.